Dual-Selective Catalysis in Dephosphorylation Tuned by Hf₆-Containing Metal-Organic Frameworks Mimicking Phosphatase.

ABSTRACT: Selective dephosphorylation is full of great challenges in the field of biomimetic catalysis. To mimic the active sites of protein phosphatase, Hf-OH-Hf motif-containing metal-organic frameworks (MOFs) were obtained and structurally characterized, which are assembled from [Hf₄₈Ni₆] cubic nanocages and exhibit good stability in various solvents and acid/base solutions. Catalytic investigations suggest as-synthesized Hf-Ni and Hf-Ni-NH ₂ display accurate type-selectivity (selectively catalyzed P-O rather than S-O or C-O bonds) and position-selectivity (selectively catalyzed phosphomonoesters over phosphodiesters) for the hydrolysis of phosphoesters. Reaction kinetic studies further revealed the high activity of the catalytic sites in these catalysts, and the unique catalytic selectivity and high activity are comparable to phosphatase. Additionally, these MOF catalysts possess good recursivity and hypotoxicity. Control experiments (including Hf- and Zr-based isomorphous MOFs) and theoretical calculations indicate that both triplet nickel and Hf₆ clusters play significant roles in the unique binding site and favorable binding energy. To our knowledge, this is the first example of selective dephosphorylation through MOF catalysts as mimic enzymes, which paves a potential way for the development of specific therapeutic MOFs.

SUBMITTER: Dong J 

PROVIDER: S-EPMC8161481 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature